Oxidative phosphorylation, electron transport and active transport of amino acids are all membrane related phenomena which require specific membrane orientation and special arrangement of the carriers involved. Some essential differences between these processes have been observed with membrane preparations which differ in spacial orientation. The differences may provide some insight into the nature of the energy transduction mechanisms which drive these processes. A complex, BCF0-BCF4 has been isolated which is required for restoration of oxidative phosphorylation. Studies are underway to determine the physical and functional properties of the components BCF0, BCF4 and the BCF0-BCF4 complex. Evidence has been obtained which indicates that trypsin treatment resulted in the removal of one of the ADP binding sites which is involved in ATP synthesis. Experiments have been designed with photoaffinity-C14 labelled ADP determine the subunit location of this site. In addition, studies will be undertaken to determine the role of the subunits in the coupling complex. Detergent treatment of the electron transport particles resulted in a loss of oxidative phosphorylation and active transport of amino acids. The addition of the purified BCF0-BCF4 complex resulted in a restoration of oxidative phosphorylation but failed to restore active transport. The addition of a crude fraction obtained following detergent treatment resulted in restoration of proline transport. Harsh detergent treatment resulted in a release of components necessary for the restoration of active transport of glutamine and glutamic acid as well as proline. Attempts will be made to purify and determine the physical and functional properties of the protein(s) component necessary for restoration of amino acid transport.